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Related Concept Videos

Integrins01:10

Integrins

Animal and protozoan cells do not have cell walls to help maintain shape and provide structural stability. Instead, these eukaryotic cells secrete a sticky mass of carbohydrates and proteins into the spaces between adjacent cells. This network of proteins and molecules is called an extracellular matrix or ECM.
Some ECM proteins assemble into a basement membrane to which the remaining components adhere. Proteoglycans typically form the bulk of the ECM while fibrous proteins, like collagen,...
Activation of Integrins01:15

Activation of Integrins

Integrins bind ligands and transmit information from outside the cell to inside or vice-versa through an "outside-in signaling" or "inside-out signaling."
In "outside-in signaling," external factors in the extracellular space bind to exposed ligand binding sites on integrins. This causes the inactive protein to undergo a conformational change to become active. Integrins are often clustered on the cell membrane. Repetitive and regularly spaced ligand binding events provide an effective stimulus.
Intracellular Signaling Affects Focal Adhesions01:17

Intracellular Signaling Affects Focal Adhesions

Integrins act both as extracellular input receivers and as intracellular processing activators. As their name suggests, integrins are entirely integrated into the membrane structure. Their hydrophobic membrane-spanning regions interact with the phospholipid bilayer's hydrophobic region. These membrane receptors provide extracellular attachment sites for effectors like hormones and growth factors. They activate intracellular response cascades when their effectors are bound and active.
Some...
Cadherins in Tissue Organization01:19

Cadherins in Tissue Organization

The cadherins are a superfamily of cell adhesion molecules comprising over 180 variants, with specific tissues expressing a particular combination of cadherin types. Cadherins generally exhibit homophilic binding; i.e., cadherins on one cell bind to cadherins of the same or closely related type on another cell. Thus, cells of the same type have a specific affinity to bind to each other and sort themselves into clusters to form tissues.
Cell Sorting During Development
Cell sorting plays an...
Renewal of Intestinal Stem Cells01:23

Renewal of Intestinal Stem Cells

The intestinal epithelial lining rapidly renews every 4 to 5 days. The renewal is facilitated by intestinal stem cells (ISCs) located at the base of the crypt– a gland located at the bottom of each villus. ISCs divide asymmetrically to form new stem cells and progenitor daughter cells. The daughter cells are called transit-amplifying (TA) cells which move upwards along the crypt and either differentiate into absorptive cells– the enterocytes or secretory cells– including the goblet,...
Role Of Notch Signalling In Intestinal Stem Cell Renewal01:12

Role Of Notch Signalling In Intestinal Stem Cell Renewal

Notch signaling was first discovered in Drosophila melanogaster, where it is involved in cell lineage differentiation. Notch signaling regulates the maintenance and differentiation of intestinal stem cells or ISCs by controlling the expression of atonal homolog 1 or Atoh1. Atoh1 directs cells to differentiate into secretory cells.
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Induced Differentiation of M Cell-like Cells in Human Stem Cell-derived Ileal Enteroid Monolayers
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Expression of integrin subunits correlates with differentiation of epithelial cell lineages in developing human

M Chénard1, J R Basque, P Chailler

  • 1Department of Anatomy and Cell Biology, Faculty of Medicine, Université de Sherbrooke, Québec, Canada.

Anatomy and Embryology
|September 20, 2000
PubMed
Summary
This summary is machine-generated.

This study reveals how specific laminin and integrin proteins guide human stomach development, particularly in differentiating mucous and chief cells. Their coordinated expression is crucial for forming functional gastric glands.

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Area of Science:

  • Developmental Biology
  • Gastroenterology
  • Cell Biology

Background:

  • Laminins, key extracellular matrix proteins, are differentially localized in human fetal gastric mucosa.
  • Integrins, cell surface receptors, mediate cell-matrix interactions crucial for tissue development.

Purpose of the Study:

  • To compare the distribution of epithelial integrin subunits and laminin alpha chains in the developing human stomach.
  • To elucidate the roles of specific laminin-integrin interactions in gastric epithelial cell differentiation.

Main Methods:

  • Indirect immunofluorescence was used to analyze tissue sections from human fetuses (8-22 weeks gestation).
  • Localization of integrin subunits (alpha2, alpha3, beta1, beta4) and laminin alpha chains (alpha1, alpha2, alpha5) was examined in different gastric regions (body, fundus, antrum).

Main Results:

  • Beta1 and alpha6 integrin subunits, along with laminin alpha1/alpha5 chains, were uniformly distributed in the epithelium.
  • Alpha3 and beta4 integrin subunits, and laminin alpha3 chain, localized to differentiating mucous cells in the surface and foveolus.
  • Alpha2 integrin subunit showed complex localization, repressed in parietal cells but increased in maturing glands, co-localizing with laminin-2 (alpha2 chain).

Conclusions:

  • Laminins and their integrin receptors are implicated in the development of all human gastric epithelial lineages.
  • Coordinated expression of alpha2 and alpha3 integrin subunits and alpha2beta1 integrin redistribution are vital for differentiating glandular secretory cells, including chief cells.